NMR spectroscopy will be used to study biochemical systems from the filamentous bacteriophages fd and Pf1. The isolated viruses and there gene 5 unwinding protein are of interest for studying virus structure, DNA packaging, and DNA-protein interactions. The virus coat protein and its precursor procoat protein will be investigated as reconstituted membrane-protein complexes. The conformational and dynamical changes of a protein in its various biological roles and physical states will be described by studying the virus gene 8 product in the form of polycrystalline procoat protein, procoat protein in aqueous solution, procoat protein in model membranes, solid coat protein, coat protein in model membranes, and the coat protein of the assembled virus. High resolution solid state NMR will be developed for use with biomolecules. Basic research into the properties and nuclear spin interactions of amino acids, peptides, proteins, and nucleic acids will be carried out in the course of investigating supramolecular structures such as viruses, DNA, DNA-protein complexes, and membrane proteins. Cross-polarization, proton-decoupling, magic angle sample spinning, multiple pulse sequences, and other NMR techniques will be fully utilized to obtain resolved signals and characterize dipole-dipole, chemical shift anisotropy, and quadrupolar interactions. These anisotropic nuclear spin interactions will be used for structure determinations of oriented samples of DNA-protein complexes.